ID A0A074VUU2_9PEZI Unreviewed; 451 AA.
AC A0A074VUU2;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Heme haloperoxidase family profile domain-containing protein {ECO:0000259|PROSITE:PS51405};
GN ORFNames=M437DRAFT_52260 {ECO:0000313|EMBL:KEQ61492.1};
OS Aureobasidium melanogenum CBS 110374.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043003 {ECO:0000313|EMBL:KEQ61492.1, ECO:0000313|Proteomes:UP000030672};
RN [1] {ECO:0000313|EMBL:KEQ61492.1, ECO:0000313|Proteomes:UP000030672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 110374 {ECO:0000313|EMBL:KEQ61492.1,
RC ECO:0000313|Proteomes:UP000030672};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|ARBA:ARBA00001970};
CC -!- SIMILARITY: Belongs to the chloroperoxidase family.
CC {ECO:0000256|ARBA:ARBA00025795}.
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DR EMBL; KL584838; KEQ61492.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074VUU2; -.
DR HOGENOM; CLU_029871_4_1_1; -.
DR OrthoDB; 1830290at2759; -.
DR Proteomes; UP000030672; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.489.10; Chloroperoxidase-like; 1.
DR InterPro; IPR000028; Chloroperoxidase.
DR InterPro; IPR036851; Chloroperoxidase-like_sf.
DR PANTHER; PTHR33577:SF16; HEME_HALOPEROXIDASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR33577; STERIGMATOCYSTIN BIOSYNTHESIS PEROXIDASE STCC-RELATED; 1.
DR Pfam; PF01328; Peroxidase_2; 1.
DR SUPFAM; SSF47571; Cloroperoxidase; 1.
DR PROSITE; PS51405; HEME_HALOPEROXIDASE; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW Reference proteome {ECO:0000313|Proteomes:UP000030672};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..451
FT /note="Heme haloperoxidase family profile domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001700921"
FT DOMAIN 87..319
FT /note="Heme haloperoxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS51405"
FT REGION 77..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 451 AA; 48039 MW; C98086BC2503EA85 CRC64;
MKFNLAIAGA VLPSVALGFP QMMGGSREDM MRMLEKRAAE EQLAKREPQI LSGVTDLLST
VVNDVRGLLE GSVAEGILNP SDKRPEPGYT FQAPGPNDSR GPCPGLNLLA NYGYLPRNGY
VNYGQVLEAT ARGFNMGTDL ATVLAVFAIL ADGDLVTESW YLGAGPNNVG GLNRHSTVEA
DISPHREDYY TGCGNNHAVS SRLVKQGVEL VAASSNKQYD MSVMAQQYAK NADFSKQYSP
YLYAFPFPQI VSLGAFAFYP NFFSNGTYGS GGVPNYESVS SIVGWKLNEN TGDFEYVPEK
WPENWYRRST PYGAVEALTD AYTQIYPSNI VVPGASTLLT PNFNATTLLC DIYQGIQSIT
PLILSGTEKD VATAVSWALG KLTPILGGGA LGCPSSDLSP EEGDILFPSA SATGGPINSP
SAQATNAGNN VYNKVYFKTA PTSPACSAGA P
//
